Literature DB >> 31707537

Structure-function relationship of H2A-H2B specific plant histone chaperones.

Ashish Kumar1,2, Dileep Vasudevan3.   

Abstract

Studies on chromatin structure and function have gained a revived popularity. Histone chaperones are significant players in chromatin organization. They play a significant role in vital nuclear functions like transcription, DNA replication, DNA repair, DNA recombination, and epigenetic regulation, primarily by aiding processes such as histone shuttling and nucleosome assembly/disassembly. Like the other eukaryotes, plants also have a highly orchestrated and dynamic chromatin organization. Plants seem to have more isoforms within the same family of histone chaperones, as compared with other organisms. As some of these are specific to plants, they must have evolved to perform functions unique to plants. However, it appears that only little effort has gone into understanding the structural features of plant histone chaperones and their structure-function relationships. Studies on plant histone chaperones are essential for understanding their role in plant chromatin organization and how plants respond during stress conditions. This review is on the structural and functional aspects of plant histone chaperone families, specifically those which bind to H2A-H2B, viz nucleosome assembly protein (NAP), nucleoplasmin (NPM), and facilitates chromatin transcription (FACT). Here, we also present comparative analyses of these plant histone chaperones with available histone chaperone structures. The review hopes to incite interest among researchers to pursue further research in the area of plant chromatin and the associated histone chaperones.

Entities:  

Keywords:  FACT; H2A-H2B; Histone chaperones; NAP1; NRP1; Nucleoplasmin

Mesh:

Substances:

Year:  2019        PMID: 31707537      PMCID: PMC6985425          DOI: 10.1007/s12192-019-01050-7

Source DB:  PubMed          Journal:  Cell Stress Chaperones        ISSN: 1355-8145            Impact factor:   3.667


  102 in total

1.  The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.

Authors:  Pascal Drané; Khalid Ouararhni; Arnaud Depaux; Muhammad Shuaib; Ali Hamiche
Journal:  Genes Dev       Date:  2010-05-26       Impact factor: 11.361

2.  HIRA and Daxx constitute two independent histone H3.3-containing predeposition complexes.

Authors:  S J Elsaesser; C D Allis
Journal:  Cold Spring Harb Symp Quant Biol       Date:  2010-11-03

Review 3.  Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.

Authors:  Christopher Warren; David Shechter
Journal:  J Mol Biol       Date:  2017-06-10       Impact factor: 5.469

Review 4.  The Evolution of HD2 Proteins in Green Plants.

Authors:  S Bourque; S Jeandroz; V Grandperret; N Lehotai; S Aimé; D E Soltis; N W Miles; M Melkonian; M K Deyholos; J H Leebens-Mack; M W Chase; C J Rothfels; D W Stevenson; S W Graham; X Wang; S Wu; J C Pires; P P Edger; Z Yan; Y Xie; E J Carpenter; G K S Wong; D Wendehenne; V Nicolas-Francès
Journal:  Trends Plant Sci       Date:  2016-10-24       Impact factor: 18.313

5.  Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays.

Authors:  T Ito; M Bulger; R Kobayashi; J T Kadonaga
Journal:  Mol Cell Biol       Date:  1996-06       Impact factor: 4.272

6.  Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.

Authors:  D Flemming Hansen; Zheng Zhou; Haniqiao Feng; Lisa M Miller Jenkins; Yawen Bai; Lewis E Kay
Journal:  J Mol Biol       Date:  2009-03-20       Impact factor: 5.469

7.  Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin.

Authors:  S L Bruhn; P M Pil; J M Essigmann; D E Housman; S J Lippard
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

8.  FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.

Authors:  David J Kemble; Laura L McCullough; Frank G Whitby; Tim Formosa; Christopher P Hill
Journal:  Mol Cell       Date:  2015-10-08       Impact factor: 17.970

9.  The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.

Authors:  Christian Edlich-Muth; Jean-Baptiste Artero; Phil Callow; Marcin R Przewloka; Aleksandra A Watson; Wei Zhang; David M Glover; Janusz Debski; Michal Dadlez; Adam R Round; V Trevor Forsyth; Ernest D Laue
Journal:  J Mol Biol       Date:  2015-03-24       Impact factor: 5.469

10.  The Phyre2 web portal for protein modeling, prediction and analysis.

Authors:  Lawrence A Kelley; Stefans Mezulis; Christopher M Yates; Mark N Wass; Michael J E Sternberg
Journal:  Nat Protoc       Date:  2015-05-07       Impact factor: 13.491

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  3 in total

1.  Phosphorylation of the FACT histone chaperone subunit SPT16 affects chromatin at RNA polymerase II transcriptional start sites in Arabidopsis.

Authors:  Philipp Michl-Holzinger; Simon Obermeyer; Hanna Markusch; Alexander Pfab; Andreas Ettner; Astrid Bruckmann; Sabrina Babl; Gernot Längst; Uwe Schwartz; Andrey Tvardovskiy; Ole N Jensen; Akihisa Osakabe; Frédéric Berger; Klaus D Grasser
Journal:  Nucleic Acids Res       Date:  2022-05-20       Impact factor: 19.160

2.  Genome-Wide Identification of NAP1 and Function Analysis in Moso Bamboo (Phyllostachys edulis).

Authors:  Yaxing Zhang; Jun Zhang; Deming Yang; Yandong Jin; Xuqing Liu; Zeyu Zhang; Lianfeng Gu; Hangxiao Zhang
Journal:  Int J Mol Sci       Date:  2022-06-10       Impact factor: 6.208

Review 3.  The FACT Histone Chaperone: Tuning Gene Transcription in the Chromatin Context to Modulate Plant Growth and Development.

Authors:  Klaus D Grasser
Journal:  Front Plant Sci       Date:  2020-02-19       Impact factor: 5.753

  3 in total

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